CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024784
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nucleoprotein TPR 
Protein Synonyms/Alias
 Megator; NPC-associated intranuclear protein; Translocated promoter region protein 
Gene Name
 Tpr 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
16LERPELNKLPKSTQNacetylation[1]
252TSNEHLQKHVEDLLTacetylation[1]
260HVEDLLTKLKEAKEQacetylation[1]
312RAVDELHKLLKEAGEacetylation[1]
345MEKEMLEKIGKLEKEacetylation[1]
348EMLEKIGKLEKELENacetylation[1]
351EKIGKLEKELENANDacetylation[1]
364NDLLSATKRKGAILSacetylation[1]
390AAVAKIVKPGMKLTEacetylation[1]
417LLEKLENKRINKYLDacetylation[1]
428KYLDEIVKEVEAKAPacetylation[1]
449EEYERAQKAVASLSAacetylation[1]
457AVASLSAKLEQAMKEacetylation[1]
457AVASLSAKLEQAMKEubiquitination[2]
474RLQEDTDKANKHSSVacetylation[1]
474RLQEDTDKANKHSSVubiquitination[3]
477EDTDKANKHSSVLERacetylation[1]
494QRMEIQIKDLSQQIRacetylation[1]
494QRMEIQIKDLSQQIRubiquitination[2]
713DLRSQNTKISTQLDFacetylation[1]
723TQLDFASKRYEMLQDacetylation[1]
748SLQERNQKLTATTQKacetylation[1]
755KLTATTQKQEQIINTacetylation[1]
755KLTATTQKQEQIINTubiquitination[2]
843RLSSQIEKLEHEISHacetylation[1]
853HEISHLKKKLENEVEacetylation[1]
854EISHLKKKLENEVEQacetylation[1]
895LNTKELLKNAQKDIAacetylation[1]
1379NEEVGRLKAEIARSNacetylation[1]
1427KIIDIQEKVKTITQVacetylation[1]
1669DPPTANIKPTPVVSTacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [3] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113] 
Functional Description
 Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs, plays a role in the establishment of nuclear-peripheral chromatin compartmentalization in interphase, and in the mitotic spindle checkpoint signaling during mitosis. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with NUP153, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Negatively regulates both the association of CTE-containing mRNA with large polyribosomes and translation initiation. Does not play any role in Rev response element (RRE)-mediated export of unspliced mRNAs. Implicated in nuclear export of mRNAs transcribed from heat shock gene promoters; associates both with chromatin in the HSP70 promoter and with mRNAs transcribed from this promoter under stress-induced conditions. Modulates the nucleocytoplasmic transport of activated MAPK1/ERK2 and huntingtin/HTT and may serve as a docking site for the XPO1/CRM1-mediated nuclear export complex. Plays also a role as a structural and functional element of the perinuclear chromatin distribution; involved in the formation and/or maintenance of NPC-associated perinuclear heterochromatin exclusion zones (HEZs). Finally, acts as a spatial regulator of the spindle-assembly checkpoint (SAC) response ensuring a timely and effective recruitment of spindle checkpoint proteins like MAD1L1 and MAD2L1 to unattached kinetochore during the metaphase-anaphase transition before chromosome congression. Its N-terminus is involved in activation of oncogenic kinases (By similarity). Plays a role in the regulation of nuclear protein export. 
Sequence Annotation
 REGION 3 13 Sufficient for interaction with TPR (By
 REGION 14 117 Necessary for interaction with HSF1 (By
 REGION 437 513 Necessary for association to the NPC (By
 REGION 1218 1320 Necessary for interaction with HSF1 (By
 REGION 1811 1866 Sufficient and essential for mediating
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 252 252 N6-acetyllysine (By similarity).
 MOD_RES 312 312 N6-acetyllysine (By similarity).
 MOD_RES 345 345 N6-acetyllysine (By similarity).
 MOD_RES 379 379 Phosphoserine (By similarity).
 MOD_RES 428 428 N6-acetyllysine (By similarity).
 MOD_RES 457 457 N6-acetyllysine (By similarity).
 MOD_RES 713 713 N6-acetyllysine (By similarity).
 MOD_RES 723 723 N6-acetyllysine (By similarity).
 MOD_RES 748 748 N6-acetyllysine (By similarity).
 MOD_RES 755 755 N6-acetyllysine (By similarity).
 MOD_RES 1185 1185 Phosphoserine (By similarity).
 MOD_RES 1691 1691 Phosphothreonine (By similarity).
 MOD_RES 2045 2045 Phosphoserine (By similarity).
 MOD_RES 2047 2047 Phosphoserine (By similarity).
 MOD_RES 2070 2070 Phosphoserine (By similarity).
 MOD_RES 2152 2152 Phosphoserine (By similarity).  
Keyword
 Acetylation; Cell cycle; Cell division; Centromere; Chromosome; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Kinetochore; Membrane; Mitosis; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport; Proto-oncogene; Reference proteome; Translocation; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2360 AA 
Protein Sequence
MAAVLQQVLE RPELNKLPKS TQNKLEKFLA EQQSEIDCLK GRHEKFKVES EQQYFEIEKR 60
LSQSQERLVN ETRECQNLRL ELEKLNNQVK VLTEKNKELE TAQDRNLGIQ SQFTRAKEEL 120
EAEKRDLIRT NERLSQEVEY LTEDVKRLNE KLKESNTTKG ELQLKLDELQ ASDVTVKYRE 180
KRLEQEKELL HNQNSWLNTE LKTKTDELLA LGREKGNEIL ELKCTLENKK EEVLRLEEQM 240
NGLKTSNEHL QKHVEDLLTK LKEAKEQQAS MEEKFHNELN AHIKLSNLYK SAADDSEAKS 300
NELTRAVDEL HKLLKEAGEA NKTIQDHLLQ VEESKDQMEK EMLEKIGKLE KELENANDLL 360
SATKRKGAIL SEEELAAMSP TAAAVAKIVK PGMKLTELYN AYVETQDQLL LEKLENKRIN 420
KYLDEIVKEV EAKAPILKRQ REEYERAQKA VASLSAKLEQ AMKEIQRLQE DTDKANKHSS 480
VLERDNQRME IQIKDLSQQI RVLLMELEEA RGNHVIRDEE VSSADISSSS EVISQHLVSY 540
RNIEELQQQN QRLLFALREL GETREREEQE TTSSKIAELQ NKLENSLTEL EQLRESRQHQ 600
MQLVDSIVRQ RDMYRILLSQ TTGMAIPLQA SSLDDISLVS TPKRSSTSQT VSTPAPEPII 660
ESTETIEAKA ALKQLQEIFE NYKKEKMDSE KLQNEQLEKL QEQVTDLRSQ NTKISTQLDF 720
ASKRYEMLQD NVEGYRREIT SLQERNQKLT ATTQKQEQII NTMTQDLRGA NEKLAVAEVR 780
AENLKKEKEM LKLSEVRLSQ QRESLLAEQR GQNLLLTNLQ TIQGILERSE TETKQRLSSQ 840
IEKLEHEISH LKKKLENEVE QRHTLTRNLD VQLLDTKRQL DTEINLHLNT KELLKNAQKD 900
IATLKQHLNN MEAQLASQST QRTGKGQPGD RDDVDDLKSQ LRQAEEQVND LKERLKTSAS 960
NVEQYRAMVT SLEDSLNKEK QVTEEVHKNI EVRLKESAEF QTQLEKKLME VEKEKQELQD 1020
DKRKAIESME QQLTELKKTL SSVQSEVQEA LQRASTALSN EQQARRDCQE QAKIAVEAQN 1080
KYERELMLHA ADVEALQAAK EQVSKMASVR QHLEETTQKA ESQLLECKAS WEERERVLKD 1140
EVSKSVSRCE DLEKQNRLLH DQIEKLSDKV VTSMKEVVQS PLNISLNEEG KSQEQILEIL 1200
RFIRREKEIA ETRFEVAQVE SLRYRQRVEL LERELQELQD SLNAEREKVQ VTAKTMAQHE 1260
ELMKKTETMN VVMETNKMLR EEKERLEQNL QQMQAKVRKL ELDILPLQEA NAELSEKSGM 1320
LQAEKKLLEE DVKRWKARNQ HLINQQKDPD TEEYRKLLSE KEIHTKRIQQ LNEEVGRLKA 1380
EIARSNASLT NNQNLIQSLK EDLSKVRTEK ESIQKDLDAK IIDIQEKVKT ITQVKKIGRR 1440
YKTQFEELKA QQKAMETSTQ SSGDHQEQHI SVQEMQELKD NLSQSETKTK SLEGQVENLQ 1500
KTLSEKETEA RSLQEQTAQL QSELSRLRQE LQDKTTKEEQ LRQQMNEKDE KTWKAITVAR 1560
SKIAHLSGVK DQLTKENEEL KQRNGALDQQ KDELDVRMTA LKSQYEGRIS RLERELREHQ 1620
ERHLEQRDEP QEPTNKAPEQ QRQITLKTTP ASGERGIAST SDPPTANIKP TPVVSTPSKV 1680
TAAAMAGNKS TPRASIRPMV TPATVTNPTT TPTATVMPTT QVESQEAMQS EGPVEHVPVF 1740
GSTSGSVRST SPNVQPSISQ PLLTVQQQTQ ATAFVQPTQQ SHPQIEPANQ ELSPNIVEVV 1800
QSSPVERPST STAVFGTVSA TPSSSLPKRA REEEEDSTIE AGDQVSDDTV EMPLPKKLKT 1860
VTPVGTEEEV MAEESTDGEA ETQTYNQDSQ DSIGEGVTQG DYTPMEDSEE TSQSLQIDLG 1920
PLQSDQQTTS SQDGQGKGDD VIVIDSDDED DDEENDGEHE DYEEDEDEDD DEEDDTGMGD 1980
EGEDSNEGTG SADGNDGYEA DDAEGGDGTD PGTETEESMG GAESNQRAAD SQNSGEGNTS 2040
AAESSFSQEV AREQQPTSAS ERQTPQAPQS PRRPPHPLPP RLTIHAPPQE LGPPVQRIQM 2100
TRRQSVGRGL QLTPGIGGMQ QHFFDDEDRT VPSTPTLVVP HRTDGFAEAI HSPQVAGVPR 2160
FRFGPPEDMP QTSSSHSDLG QLASQGGLGM YETPLFLAHE EESGGRSVPT TPLQVAAPVT 2220
VFTESTTSDA SEHASQSVPM VTTSTGTLST TNETPAGDDG DEVFVETESE GISSEAGLEI 2280
DSQQEEEPVQ ASDESDLPST SQDPPSSSSV DTSSSQPKPF RRVRLQTTLR QGVRGRQFNR 2340
QRGISHAMGG RGGINRGNIN 2360 
Gene Ontology
 GO:0005868; C:cytoplasmic dynein complex; ISS:UniProtKB.
 GO:0019898; C:extrinsic to membrane; ISS:UniProtKB.
 GO:0000776; C:kinetochore; ISS:UniProtKB.
 GO:0072686; C:mitotic spindle; ISS:UniProtKB.
 GO:0042405; C:nuclear inclusion body; IDA:UniProtKB.
 GO:0031965; C:nuclear membrane; IDA:UniProtKB.
 GO:0034399; C:nuclear periphery; IDA:UniProtKB.
 GO:0044615; C:nuclear pore nuclear basket; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0003682; F:chromatin binding; ISS:UniProtKB.
 GO:0031072; F:heat shock protein binding; ISS:UniProtKB.
 GO:0051019; F:mitogen-activated protein kinase binding; ISS:UniProtKB.
 GO:0003729; F:mRNA binding; ISS:UniProtKB.
 GO:0005487; F:nucleocytoplasmic transporter activity; ISS:UniProtKB.
 GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
 GO:0004828; F:serine-tRNA ligase activity; IEA:InterPro.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0035457; P:cellular response to interferon-alpha; ISS:UniProtKB.
 GO:0000189; P:MAPK import into nucleus; ISS:UniProtKB.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0007094; P:mitotic spindle assembly checkpoint; ISS:UniProtKB.
 GO:0031990; P:mRNA export from nucleus in response to heat stress; ISS:UniProtKB.
 GO:0046832; P:negative regulation of RNA export from nucleus; ISS:UniProtKB.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
 GO:0045947; P:negative regulation of translational initiation; ISS:UniProtKB.
 GO:0006999; P:nuclear pore organization; ISS:UniProtKB.
 GO:0031453; P:positive regulation of heterochromatin assembly; ISS:UniProtKB.
 GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; ISS:UniProtKB.
 GO:0046827; P:positive regulation of protein export from nucleus; IMP:UniProtKB.
 GO:0042307; P:positive regulation of protein import into nucleus; ISS:UniProtKB.
 GO:0010965; P:regulation of mitotic sister chromatid separation; ISS:UniProtKB.
 GO:1901673; P:regulation of spindle assembly involved in mitosis; ISS:UniProtKB.
 GO:0070849; P:response to epidermal growth factor stimulus; ISS:UniProtKB.
 GO:0006404; P:RNA import into nucleus; ISS:UniProtKB.
 GO:0006434; P:seryl-tRNA aminoacylation; IEA:InterPro. 
Interpro
 IPR009053; Prefoldin.
 IPR015866; Ser-tRNA-synth_1_N.
 IPR012929; TPR_MLP1_2. 
Pfam
 PF07926; TPR_MLP1_2 
SMART
  
PROSITE
  
PRINTS